ArticleMolecular and cellular biology1999
Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 194 citations in OpenAlex.
- Genomic Insights intoJournal of fungi (Basel, Switzerland) · 2026Article
- Tethering of cellulose synthase complex to the plasma membrane relies on the isoform of EXO70A1 in Arabidopsis.Scientific reports · 2024Article
- Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024Review
- The exocyst in context.Biochemical Society transactions · 2024Review
- Septin-mediated RhoA activation engages the exocyst complex to recruit the cilium transition zone.The Journal of cell biology · 2023Article
- An isoform-specific function of Cdc42 in regulating mammalian Exo70 during axon formation.Life science alliance · 2023Article
- High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane ineLife · 2022Article
- Transcriptomic Dynamics of Active and Inactive States of Rho GTPase MoRho3 inJournal of fungi (Basel, Switzerland) · 2022Article
- Cancer cells resist antibody-mediated destruction by neutrophils through activation of the exocyst complex.Journal for immunotherapy of cancer · 2022Article
- The Small GTPase CsRAC1 Is Important for Fungal Development and Pepper Anthracnose in Colletotrichum scovillei.The plant pathology journal · 2021Article
- Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Polarized Redistribution of the Contractile Vacuole to the Rear of the Cell is Critical for Streaming and is Regulated by PI(4,5)P2-Mediated Exocytosis.Frontiers in cell and developmental biology · 2021Review
- Comparative Proteomics Analysis Reveals Unique Early Signaling Response ofInternational journal of molecular sciences · 2020Article
- Yeast Rgd3 is a phospho-regulated F-BAR-containing RhoGAP involved in the regulation of Rho3 distribution and cell morphology.Molecular biology of the cell · 2020Article
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- The role of the exocyst in renal ciliogenesis, cystogenesis, tubulogenesis, and development.Kidney research and clinical practice · 2019Review
- The Cdc42 effectors Gic1 and Gic2 regulate polarized post-Golgi secretion.Cell & bioscience · 2019Article
- Regulation of Cell Polarity by Exocyst-Mediated Trafficking.Cold Spring Harbor perspectives in biology · 2018Review
- Exocyst Subunit EXO70H4 Has a Specific Role in Callose Synthase Secretion and Silica Accumulation.Plant physiology · 2018Article
- Polarized Exocytosis.Cold Spring Harbor perspectives in biology · 2017Review
26 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The Rho3 protein plays a critical role in the budding yeast Saccharomyces cerevisiae by directing proper cell growth. Rho3 appears to influence cell growth by regulating polarized secretion and the actin cytoskeleton, since rho3 mutants exhibit large rounded cells with an aberrant actin cytoskeleton. To gain insights into how Rho3 influences these events, we have carried out a yeast two-hybrid screen using an S. cerevisiae cDNA library to identify proteins interacting with Rho3. Two proteins, Exo70 and Myo2, were identified in this screen. Interactions with these two proteins are greatly reduced or abolished when mutations are introduced into the Rho3 effector domain. In addition, a type of mutation known to produce dominant negative mutants of Rho proteins abolished the interaction with both of these proteins. In contrast, Rho3 did not interact with protein kinase C (Pkc1), an effector of another Rho family protein, Rho1, nor did Rho1 interact with Exo70 or Myo2. Rho3 did interact with Bni1, another effector of Rho1, but less efficiently than with Rho1. The interaction between Rho3 and Exo70 and between Rho3 and Myo2 was also demonstrated with purified proteins. The interaction between Exo70 and Rho3 in vitro was dependent on the presence of GTP, since Rho3 complexed with guanosine 5'-O-(3-thiotriphosphate) interacted more efficiently with Exo70 than Rho3 complexed with guanosine 5'-O-(3-thiodiphosphate). Overlapping subcellular localization of the Rho3 and Exo70 proteins was demonstrated by indirect immunofluorescence. In addition, patterns of localization of both Exo70 and Rho3 were altered when a dominant active allele of RHO3, RHO3(E129,A131), which causes a morphological abnormality, was expressed. These results provide a direct molecular basis for the action of Rho3 on exocytosis and the actin cytoskeleton.
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